The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.
The N‐end rule pathway of protein degradation
Open accessAbstract
The N‐end rule relates the in vivo half‐life of a protein to the identity of its N‐terminal residue. Similar but distinct versions of the N‐end rule operate in all organisms examined, from mammals to fungi and bacteria. In eukaryotes, the N‐end rule pathway is a part of the ubiquitin system. Ubiquitin is a 76‐residue protein whose covalent conjugation to other proteins plays a role in many biological processes, including cell growth and differentiation. I discuss the current understanding of the N‐end rule pathway.
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Cites
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Self-citationCommon Principles of Protein Translocation Across Membranes
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Self-citationA Proteolytic Pathway That Recognizes Ubiquitin as a Degradation Signal
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Cited by
Hershko, A., Ciechanover, A., & Varshavsky, A. (2000) · Nature Medicine · doi:10.1038/80384 · Cited by 649
Self-citationTanida, I., Tanida-Miyake, E., Ueno, T., & Kominami, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000752200 · Cited by 344
Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease
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Regulation of Human Separase by Securin Binding and Autocleavage
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Molecular regulation of muscle cachexia: it may be more than the proteasome.
Hasselgren, P.-O., Wray, C., & Mammen, J. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5849 · Cited by 146
Metadata
- Authors
- Varshavsky, A.
- Venue
- Genes to Cells
- Publisher
- Wiley
- Published
- 1997-01
- Volume
- 2
- Issue
- 1
- Pages
- 13-28
- ISSN
- 1356-9597 (ISSN-L)
- 1365-2443
- OpenAlex
- W2166080631
- Cited by
- 367
- References
- 70
- FWCI
- 4.61
- Type
- journal article
- Language
- en
- Open access
- bronze
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